Function of the Mos/MAPK pathway during oocyte maturation in the Japanese brown frogRana japonica

Yoshida, Noriyuki; Mita, Koichi; Yamashita, Masakane

doi:10.1002/1098-2795(200009)57:1<88::aid-mrd12>3.0.co;2-9

Cited by 21 publications

(11 citation statements)

References 79 publications

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“…In vertebrates, resumption of meiosis after prophase I arrest in oocytes is triggered by a pituitary luteinizing hormone (LH) surge, which stimulates the synthesis of a maturation-inducing substance (MIS) in the ovary (Jalabert et al, 1991;Kagawa, 1994;Nagahama, 1997;Yamashita, 1998;Thomas, 1994;Thomas, 1999;Yoshida et al, 2000;Patino et al, 2001). In teleosts, chemically different molecules have been demonstrated to elicit MIS activity and they include 17,20␤-dihydroxy-4-pregnen-3-one (17,20␤-DP), 17,20␤,21-trihydroxy-4-pregnen-3-one (17␤-S), corticosteroids, insulin, insulin-like growth factors and activin (Scott and Canario, 1987;Nagahama, 1997;Tyler et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

2-hydroxyestradiol-17β-induced oocyte maturation: involvement of cAMP–protein kinase A and okadaic acid-sensitive protein phosphatases,and their interplay in oocyte maturation in the catfishHeteropneustes fossilis

Mishra

Joy

2006

Journal of Experimental Biology

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SUMMARY In Heteropneustes fossilis, in vitro incubation of postvitellogenic follicles with 2-hydroxyestradiol-17β(2-OHE2, 5 μmol l–1) decreased significantly the total cAMP level, concomitant with germinal vesicle breakdown (GVBD). The incubation of the follicles with cAMP or cAMP-elevating drugs[phosphodiesterase (PDE) inhibitors], such as IBMX(3-isobutyl-1-methyl-xanthine), theophylline and caffeine, inhibited the 2-OHE2-induced GVBD in a concentration-dependent manner. The magnitude of the response varied: both cAMP and IBMX were effective at all concentrations (0.1–2.0 mmol l–1), followed by theophylline (0.5–2.0 mmol l–1) and caffeine(1–2.0 mmol l–1). The protein kinase A (PKA) inhibitor H89 stimulated oocyte maturation in a concentration-dependent manner. However,when co-incubated with 2-OHE2 for 24 h it produced a biphasic effect: low concentrations (0.1 and 1.0 μmol l–1) did not alter the 2-OHE2-induced GVBD, but high concentrations (5 and 10μmol l–1) inhibited it. The incubation of the follicles with H89 lowered the inhibitory effect of IBMX on the 2-OHE2-induced GVBD. The incubation of the follicles with okadaic acid (OA), a protein phosphatase 1 and 2A inhibitor did not affect GVBD but when co-incubated with 2-OHE2, it enhanced the GVBD response. OA reversed the inhibitory effect of IBMX. The results suggest that OA may overcome the inhibition of 2-OHE2-induced GVBD by IBMX at a step distal to the cAMP–PKA pathway.

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Section: Introductionmentioning

confidence: 99%

2-hydroxyestradiol-17β-induced oocyte maturation: involvement of cAMP–protein kinase A and okadaic acid-sensitive protein phosphatases,and their interplay in oocyte maturation in the catfishHeteropneustes fossilis

Mishra

Joy

2006

Journal of Experimental Biology

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“…The mos protein is a serine/threonine protein kinase (Maxwell and Arlinghaus, 1985;Paules et al, 1992;Singh et al, 1988) that plays an essential role in the maturation of oocytes, where it is required for the activation of the maturation promoting factor (MPF) (de Moor and Richter, 1997;Yoshida et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Double-stranded RNA-dependent protein kinase, PKR, down-regulates CDC2/cyclin B1 and induces apoptosis in non-transformed but not in v-mos transformed cells

et al. 2001

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The interferon (IFN)-induced, double stranded RNA (dsRNA)-activated serine/threonine kinase, PKR, is a potent negative regulator of cell growth when overexpressed in yeast or mammalian cells. Paradoxically, while it can function as a tumor suppressor and inducer of apoptosis, it is overexpressed in a variety of human cancers. To resolve this enigma, we established cell-lines that overexpress PKR in non-transformed and in v-mos transformed CHO cells. Overexpression of PKR suppressed the proliferation of CHO cells by inducing a transient G0/G1 arrest, followed by a delayed G2/M arrest, which attenuated cell cycle progression. These e ects were accompanied by early induction of p21/ WAF-1 and delayed downregulation of CDC2 and cyclin B1. Induction of proapoptotic activity of the ectopic PKR paralleled the onset of G2/M arrest in CHO cells. However, while transiently inducing p21/WAF-1, PKR did not impose G2/M arrest or apoptosis in v-mostransformed cells, nor was CDC2 or cyclin B1 downregulated in those cells. These ®ndings link the proapoptotic activity of PKR to the arrest of cell cycle at the G2/M phase. Consequently, the apoptotic activity of PKR could be counter-acted by an oncogene-like vmos that overrides the G2/M arrest induced by PKR. Oncogene (2001) 20, 8045 ± 8056.

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“…One of these kinases is the family of mitogenactivated/microtubule-associated protein kinases (MAPK) (Ruderman 1993). MAPK is activated during oocyte maturation in mammals (Sobajima et al 1993;Inoue et al 1995;Didieu et al 1996;Fissore et al 1996;Goudet et al 1998;Sun et al 1999), frogs (Ferrell et al 1991;Gotoh et al 1991a, b;Yoshida et al 2000) and marine invertebrates (Sanghera et al 1990;Shibuya et al 1992;Eckberg 1997;Russo et al 1998;Gould and Stephano 1999). MAPK is a serine/threonine kinase that requires dual phosphorylation on threonine and tyrosine residues for full activation (Posada and Cooper 1992).…”

Section: Introductionmentioning

confidence: 99%

The Mos/MAPK pathway is involved in metaphase II arrest as a cytostatic factor but is neither necessary nor sufficient for initiating oocyte maturation in goldfish

Kajiura-Kobayashi

Yoshida²,

Sagata

et al. 2000

Development Genes and Evolution

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Mos plays a crucial role in meiotic cell division in vertebrates. In Xenopus, Mos is involved in the initiation of oocyte maturation as an initiator and in the arrest at the metaphase II stage (MII) as a component of the cytostatic factor (CSF). The function of Mos is mediated by MAP kinase (MAPK). We investigated the function of the Mos/MAPK pathway during goldfish oocyte maturation induced by 17alpha,20beta-dihydroxy-4-pregnen-3-one (17alpha,20beta-DP), a natural maturation-inducing hormone in fishes. Mos was absent in immature goldfish oocytes. It appeared before the onset of germinal vesicle breakdown (GVBD), increased to a maximum in mature oocytes arrested at MII and disappeared after fertilization. MAPK was activated after Mos synthesis but before maturation-promoting factor (MPF) activation, and its activity reached maximum at MII. Injection of either Xenopus or goldfish c-mos mRNA into one blastomere of 2-cell-stage Xenopus and goldfish embryos induced metaphase arrest, suggesting that goldfish Mos has a CSF activity. Injection of constitutively active Xenopus c-mos mRNA into immature goldfish oocytes induced MAPK activation, but neither MPF activation nor GVBD occurred. Conversely, the injection of goldfish c-mos antisense RNA inhibited both Mos synthesis and MAPK activation in the 17alpha,20beta-DP-treated oocytes, but these oocytes underwent GVBD. These results indicate that the Mos/MAPK pathway is not essential for initiating goldfish oocyte maturation despite its general function as a CSF. We discuss the general role of Mos/MAPK during oocyte maturation, with reference to the difference in contents of inactive MPF (pre-MPF) stored in immature oocytes.

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Function of the Mos/MAPK pathway during oocyte maturation in the Japanese brown frogRana japonica

Cited by 21 publications

References 79 publications

2-hydroxyestradiol-17β-induced oocyte maturation: involvement of cAMP–protein kinase A and okadaic acid-sensitive protein phosphatases,and their interplay in oocyte maturation in the catfishHeteropneustes fossilis

2-hydroxyestradiol-17β-induced oocyte maturation: involvement of cAMP–protein kinase A and okadaic acid-sensitive protein phosphatases,and their interplay in oocyte maturation in the catfishHeteropneustes fossilis

Double-stranded RNA-dependent protein kinase, PKR, down-regulates CDC2/cyclin B1 and induces apoptosis in non-transformed but not in v-mos transformed cells

The Mos/MAPK pathway is involved in metaphase II arrest as a cytostatic factor but is neither necessary nor sufficient for initiating oocyte maturation in goldfish

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